CONICET | Buscador de Institutos y Recursos Humanos

In the area of biomedicine, the use of nanoparticles (NPs) as carriers of therapeutic or theranostic agents has increased in the last years. Therefore, it is mandatory to understand the interaction between NPs and living organisms. In contact with biological fluids, the surface of NPs (synthetic identity) is covered with biomolecules (mainly proteins) that form a protein corona, which defines the biological identity. The protein corona formation is mediated by non-specific physical interactions, common to all molecular systems (van der Waals, electrostatics, etc.) as well as protein-protein interactions (PPI). This work is aimed at studying the protein corona formation on layered double hydroxides nanoparticles (LDH-NPs) previously modified with either albumin (LDH@ALB) or fetal bovine serum (LDH@FBS) and the cellular response of the biological identity. With such a purpose, LDH@ALB and LDH@FBS were dispersed in a protein containing cell culture medium, to compare the interfacial properties of the synthetic and biological identities and to characterize the protein corona. The interfacial properties were determined by dynamic light scattering measuring the size distribution and zeta potential. The molecules of the protein corona were identified by liquid chromatography coupled to mass spectrometry and the PPI network was evaluated with a novel approach, based on the bioinformatic tool STRING v.10.0 (http: //www.string-db.org/). The cellular response was evaluated through cytotoxicity and internalization experiments. We demonstrate that the protein corona formation was guided by PPI, through bioaffinity recognition, which led to different networks depending on the surface properties, defined by the protein coating. Furthermore, LDH@ALB and LDH@FBS are not cytotoxic and both present high levels of cellular internalization.